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J. Biol. Chem., Vol. 275, Issue 29, 22121-22126, July 21, 2000
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From The Wellcome Trust Biocentre, Department of Biochemistry,
University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Here we characterize the properties and
expression pattern of Siglec-9 (sialic acid-binding
Ig-like lectin-9), a new member of the Siglec
subgroup of the immunoglobulin superfamily. A full-length cDNA
encoding Siglec-9 was isolated from a dibutyryl cAMP-treated HL-60 cell
cDNA library. Siglec-9 is predicted to contain three extracellular
immunoglobulin-like domains that comprise an N-terminal V-set domain
and two C2-set domains, a transmembrane region and a cytoplasmic tail
containing two putative tyrosine-based signaling motifs. Overall,
Siglec-9 is ~80% identical in amino acid sequence to Siglec-7,
suggesting that the genes encoding these two proteins arose relatively
recently by gene duplication. Binding assays showed that, similar to
Siglec-7, Siglec-9 recognized sialic acid in either the The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF247180.
Siglec-9, a Novel Sialic Acid Binding Member of the
Immunoglobulin Superfamily Expressed Broadly on Human Blood
Leukocytes*
,
2,3- or
2,6-glycosidic linkage to galactose. Using a specific mAb, Siglec-9
was found to be expressed at high or intermediate levels by monocytes,
neutrophils, and a minor population of CD16+,
CD56
cells. Weaker expression was observed on ~50% of
B cells and NK cells and minor subsets of CD8+ T cells and
CD4+ T cells. These results show that despite their high
degree of sequence similarity, Siglec-7 and Siglec-9 have distinct
expression profiles.
*
This work was supported in part by the Wellcome Trust and
the Human Frontiers Science Program.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a Medical Research Council studentship.
§
To whom correspondence should be addressed: MSI/WTB Complex, Dept.
of Biochemistry, University of Dundee, Dow Street, Dundee DD1 5EH,
Scotland, United Kingdom. Tel.: 44-1382-345781; Fax: 44-1382-345855;
E-mail: p.r.crocker@dundee.ac.uk.
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